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Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus.
J Mol Biol. 2000 Apr 14; 297(5):1031-6.JM

Abstract

We have determined the three-dimensional structure of 6, 7-dimethyl-8-ribityllumazine synthase (lumazine synthase) from Brucella abortus, the infectious organism of the disease brucellosis in animals. This enzyme catalyses the formation of 6, 7-dimethyl-8-ribityllumazine, the penultimate product in the synthesis of riboflavin. The three-dimensional X-ray crystal structure of the enzyme from B. abortus has been solved and refined at 2.7 A resolution to a final R-value of 0.18 (R(free)=0.23). The macromolecular assembly of the enzyme differs from that of the enzyme from Bacillus subtilis, the only other lumazine synthase structure known. While the protein from B. subtilis assembles into a 60 subunit icosahedral capsid built from 12 pentameric units, the enzyme from B. abortus is pentameric in its crystalline form. Nonetheless, the active sites of the two enzymes are virtually identical indicating inhibitors to theses enzymes could be effective pharmaceuticals across a broad species range. Furthermore, we compare the structures of the enzyme from B. subtilis and B. abortus and describe the C teminus structure which accounts for the differences in quaternary structure.

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Authors+Show Affiliations

Braden BC
Department of Natural Sciences, Bowie State University, Bowie, MD, USA. bbraden@bowiestate.edu
Velikovsky CA
No affiliation info available
Cauerhff AA
No affiliation info available
Polikarpov I
No affiliation info available
Goldbaum FA
No affiliation info available

MeSH

Bacillus subtilisBinding SitesBrucella abortusCrystallography, X-RayHydrogen BondingModels, MolecularMolecular Sequence DataMultienzyme ComplexesProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiarySequence Homology, Amino Acid

Pub Type(s)

Comparative Study
Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

10764570

Citation

Braden, B C., et al. "Divergence in Macromolecular Assembly: X-ray Crystallographic Structure Analysis of Lumazine Synthase From Brucella Abortus." Journal of Molecular Biology, vol. 297, no. 5, 2000, pp. 1031-6.
Braden BC, Velikovsky CA, Cauerhff AA, et al. Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus. J Mol Biol. 2000;297(5):1031-6.
Braden, B. C., Velikovsky, C. A., Cauerhff, A. A., Polikarpov, I., & Goldbaum, F. A. (2000). Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus. Journal of Molecular Biology, 297(5), 1031-6.
Braden BC, et al. Divergence in Macromolecular Assembly: X-ray Crystallographic Structure Analysis of Lumazine Synthase From Brucella Abortus. J Mol Biol. 2000 Apr 14;297(5):1031-6. PubMed PMID: 10764570.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Divergence in macromolecular assembly: X-ray crystallographic structure analysis of lumazine synthase from Brucella abortus. AU - Braden,B C, AU - Velikovsky,C A, AU - Cauerhff,A A, AU - Polikarpov,I, AU - Goldbaum,F A, PY - 2000/4/15/pubmed PY - 2000/4/15/medline PY - 2000/4/15/entrez SP - 1031 EP - 6 JF - Journal of molecular biology JO - J Mol Biol VL - 297 IS - 5 N2 - We have determined the three-dimensional structure of 6, 7-dimethyl-8-ribityllumazine synthase (lumazine synthase) from Brucella abortus, the infectious organism of the disease brucellosis in animals. This enzyme catalyses the formation of 6, 7-dimethyl-8-ribityllumazine, the penultimate product in the synthesis of riboflavin. The three-dimensional X-ray crystal structure of the enzyme from B. abortus has been solved and refined at 2.7 A resolution to a final R-value of 0.18 (R(free)=0.23). The macromolecular assembly of the enzyme differs from that of the enzyme from Bacillus subtilis, the only other lumazine synthase structure known. While the protein from B. subtilis assembles into a 60 subunit icosahedral capsid built from 12 pentameric units, the enzyme from B. abortus is pentameric in its crystalline form. Nonetheless, the active sites of the two enzymes are virtually identical indicating inhibitors to theses enzymes could be effective pharmaceuticals across a broad species range. Furthermore, we compare the structures of the enzyme from B. subtilis and B. abortus and describe the C teminus structure which accounts for the differences in quaternary structure. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/10764570/Divergence_in_macromolecular_assembly:_X_ray_crystallographic_structure_analysis_of_lumazine_synthase_from_Brucella_abortus_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(00)93640-4 DB - PRIME DP - Unbound Medicine ER -